Study of the Binding between Camptothecin Analogs and FTO by Spectroscopy and Molecular Docking

被引:26
|
作者
Ren, Ting [1 ]
Wang, Zechun [1 ]
Zhang, Lijiao [1 ]
Wang, Ning [1 ]
Han, Xinxin [1 ]
Wang, Ruiyong [1 ]
Chang, Junbiao [1 ]
机构
[1] Zhengzhou Univ, Coll Chem & Mol Engn, 100 Sci Ave, Zhengzhou 450001, Peoples R China
基金
中国国家自然科学基金;
关键词
FTO; Camptothecin analogs; Fluorescence; Binding; Molecular modeling; BOVINE SERUM-ALBUMIN; FLUORESCENCE SPECTROSCOPY; TOPOISOMERASE-I; DNA-BINDING; FAT MASS; DERIVATIVES; OXYGEN; MODE; GENE;
D O I
10.1007/s10895-017-2086-2
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
In this work, the interaction between camptothecin (CPT) analogs and fat mass and obesity associated (FTO) was investigated using spectroscopy and molecular docking. From the experimental results, it was found that the CPT analogs caused the fluorescence quenching of FTO through a static quenching procedure. The binding constants and thermodynamic parameters at three different temperatures, the number of binding sites were obtained, which suggested that the hydrophobic interaction and electrostatic force played major role in the reaction between CPT analogs and FTO. Results revealed that 10-hydroxycamptothecin was the strongest quencher.
引用
收藏
页码:1467 / 1477
页数:11
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